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https://olympias.lib.uoi.gr/jspui/handle/123456789/9663Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Gerothanassis, I. P. | en |
| dc.date.accessioned | 2015-11-24T16:50:56Z | - |
| dc.date.available | 2015-11-24T16:50:56Z | - |
| dc.identifier.issn | 0006-3525 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/9663 | - |
| dc.rights | Default Licence | - |
| dc.subject | o-17 shielding | en |
| dc.subject | o-17 line widths | en |
| dc.subject | hydrogen bonding | en |
| dc.subject | nmr time scale | en |
| dc.subject | chemical-shifts | en |
| dc.subject | model peptides | en |
| dc.subject | beta-turns | en |
| dc.subject | nmr | en |
| dc.subject | spectroscopy | en |
| dc.subject | proteins | en |
| dc.subject | hydration | en |
| dc.subject | amides | en |
| dc.subject | isomers | en |
| dc.subject | tool | en |
| dc.title | The O-17-NMR shielding range and shielding time scale and detection of discrete hydrogen-bonded conformational states in peptides | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.primary | Doi 10.1002/1097-0282(200109)59:3<125::Aid-Bip1012>3.0.Co;2-A | - |
| heal.identifier.secondary | <Go to ISI>://000169783600001 | - |
| heal.identifier.secondary | http://onlinelibrary.wiley.com/store/10.1002/1097-0282(200109)59:3<125::AID-BIP1012>3.0.CO;2-A/asset/1012_ftp.pdf?v=1&t=hmn3k9s5&s=d9309a24435c4b8697b89e5e5ba39fd9d28835b1 | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
| heal.publicationDate | 2001 | - |
| heal.abstract | The O-17-NMR shielding range and shielding time scale due to hydrogen-bonding interactions in peptides are critically evaluated relative to those of H-1-NMR. Furthermore, the assumptions and conclusions in previous O-17-NMR studies on the detection of discrete conformational states in peptides (V. Tsikaris et al., Biopolymers, 2000, Vol. 53, pp. 135-139) are reconsidered. Consistent examination of the method demonstrates that although O-17 shieldings of peptide oxygens are very sensitive to hydrogen bonding interactions, the O-17-NMR shielding time scale is not advantageous compared to that of H-1-NMR, and thus it is not suitable for the detection of discrete hydrogen-bonded conformational states in peptides. O-17-NMR spectroscopy is prone to interpretation errors due to the formation of O-17-labeled impurities during the synthetic procedures (A. Steinschneider et al., International Journal of Peptide and Protein Research, 1981, Vol. 18 pp. 324-333). (C) 2001 John Wiley & Sons, Inc. | en |
| heal.publisher | Wiley-Blackwell | en |
| heal.journalName | Biopolymers | en |
| heal.journalType | peer reviewed | - |
| heal.fullTextAvailability | TRUE | - |
| Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| Gerothanassis-2001-The O-17-NMR shieldi.pdf | 80.47 kB | Adobe PDF | View/Open Request a copy |
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